| UniProt ID | BMH1_YEAST | |
|---|---|---|
| UniProt AC | P29311 | |
| Protein Name | Protein BMH1 | |
| Gene Name | BMH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 267 | |
| Subcellular Localization | ||
| Protein Description | Involved in growth regulation.. | |
| Protein Sequence | MSTSREDSVYLAKLAEQAERYEEMVENMKTVASSGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESKEKSEHQVELICSYRSKIETELTKISDDILSVLDSHLIPSATTGESKVFYYKMKGDYHRYLAEFSSGDAREKATNASLEAYKTASEIATTELPPTHPIRLGLALNFSVFYYEIQNSPDKACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMSESGQAEDQQQQQQHQQQQPPAAAEGEAPK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSTSREDSV ------CCCCHHHHH | 34.78 | 9298649 | |
| 2 | Phosphorylation | ------MSTSREDSV ------CCCCHHHHH | 34.78 | 22369663 | |
| 3 | Phosphorylation | -----MSTSREDSVY -----CCCCHHHHHH | 30.42 | 22369663 | |
| 4 | Phosphorylation | ----MSTSREDSVYL ----CCCCHHHHHHH | 26.77 | 22369663 | |
| 8 | Phosphorylation | MSTSREDSVYLAKLA CCCCHHHHHHHHHHH | 14.12 | 22369663 | |
| 10 | Phosphorylation | TSREDSVYLAKLAEQ CCHHHHHHHHHHHHH | 12.61 | 22369663 | |
| 13 | Ubiquitination | EDSVYLAKLAEQAER HHHHHHHHHHHHHHH | 45.71 | 24961812 | |
| 13 | Acetylation | EDSVYLAKLAEQAER HHHHHHHHHHHHHHH | 45.71 | 24489116 | |
| 47 | Phosphorylation | VEERNLLSVAYKNVI HHHHHHHHHHHHHHH | 14.10 | 22369663 | |
| 50 | Phosphorylation | RNLLSVAYKNVIGAR HHHHHHHHHHHHCHH | 10.84 | 22369663 | |
| 51 | Acetylation | NLLSVAYKNVIGARR HHHHHHHHHHHCHHH | 34.69 | 24489116 | |
| 51 | Ubiquitination | NLLSVAYKNVIGARR HHHHHHHHHHHCHHH | 34.69 | 23749301 | |
| 51 | Succinylation | NLLSVAYKNVIGARR HHHHHHHHHHHCHHH | 34.69 | 23954790 | |
| 65 | Phosphorylation | RASWRIVSSIEQKEE HHHHHHHHHHHHHHH | 24.19 | 22369663 | |
| 66 | Phosphorylation | ASWRIVSSIEQKEES HHHHHHHHHHHHHHH | 21.17 | 24909858 | |
| 70 | Acetylation | IVSSIEQKEESKEKS HHHHHHHHHHHHCCC | 51.13 | 24489116 | |
| 70 | Ubiquitination | IVSSIEQKEESKEKS HHHHHHHHHHHHCCC | 51.13 | 23749301 | |
| 70 | Succinylation | IVSSIEQKEESKEKS HHHHHHHHHHHHCCC | 51.13 | 23954790 | |
| 73 | Phosphorylation | SIEQKEESKEKSEHQ HHHHHHHHHCCCHHH | 47.40 | 22369663 | |
| 74 | Ubiquitination | IEQKEESKEKSEHQV HHHHHHHHCCCHHHH | 72.88 | 22817900 | |
| 74 | Acetylation | IEQKEESKEKSEHQV HHHHHHHHCCCHHHH | 72.88 | 24489116 | |
| 76 | Acetylation | QKEESKEKSEHQVEL HHHHHHCCCHHHHHH | 65.95 | 24489116 | |
| 76 | Ubiquitination | QKEESKEKSEHQVEL HHHHHHCCCHHHHHH | 65.95 | 23749301 | |
| 86 | Phosphorylation | HQVELICSYRSKIET HHHHHHHHHHHHHHH | 19.31 | 17287358 | |
| 89 | Phosphorylation | ELICSYRSKIETELT HHHHHHHHHHHHHHH | 29.74 | 17287358 | |
| 90 | Acetylation | LICSYRSKIETELTK HHHHHHHHHHHHHHH | 35.25 | 22865919 | |
| 99 | Phosphorylation | ETELTKISDDILSVL HHHHHHCCHHHHHHH | 30.68 | 21440633 | |
| 104 | Phosphorylation | KISDDILSVLDSHLI HCCHHHHHHHHHCCC | 22.44 | 22369663 | |
| 108 | Phosphorylation | DILSVLDSHLIPSAT HHHHHHHHCCCCCCC | 18.94 | 22369663 | |
| 113 | Phosphorylation | LDSHLIPSATTGESK HHHCCCCCCCCCCCE | 31.11 | 22369663 | |
| 115 | Phosphorylation | SHLIPSATTGESKVF HCCCCCCCCCCCEEE | 39.40 | 22369663 | |
| 116 | Phosphorylation | HLIPSATTGESKVFY CCCCCCCCCCCEEEE | 38.37 | 21440633 | |
| 119 | Phosphorylation | PSATTGESKVFYYKM CCCCCCCCEEEEEEE | 35.15 | 22369663 | |
| 125 | Succinylation | ESKVFYYKMKGDYHR CCEEEEEEECCCHHH | 23.82 | 23954790 | |
| 125 | Acetylation | ESKVFYYKMKGDYHR CCEEEEEEECCCHHH | 23.82 | 24489116 | |
| 145 | Ubiquitination | SSGDAREKATNASLE CCCCHHHHHHHHHHH | 55.76 | 23749301 | |
| 145 | Acetylation | SSGDAREKATNASLE CCCCHHHHHHHHHHH | 55.76 | 22865919 | |
| 155 | Acetylation | NASLEAYKTASEIAT HHHHHHHHHHHHHHC | 44.66 | 24489116 | |
| 198 | Acetylation | DKACHLAKQAFDDAI CHHHHHHHHHHHHHH | 48.82 | 25381059 | |
| 210 | Phosphorylation | DAIAELDTLSEESYK HHHHHHHCCCHHHCC | 44.82 | 22369663 | |
| 212 | Phosphorylation | IAELDTLSEESYKDS HHHHHCCCHHHCCCH | 41.22 | 22369663 | |
| 215 | Phosphorylation | LDTLSEESYKDSTLI HHCCCHHHCCCHHHH | 33.17 | 22369663 | |
| 216 | Phosphorylation | DTLSEESYKDSTLIM HCCCHHHCCCHHHHH | 23.30 | 22369663 | |
| 219 | Phosphorylation | SEESYKDSTLIMQLL CHHHCCCHHHHHHHH | 22.44 | 19779198 | |
| 220 | Phosphorylation | EESYKDSTLIMQLLR HHHCCCHHHHHHHHH | 30.36 | 22369663 | |
| 231 | Phosphorylation | QLLRDNLTLWTSDMS HHHHCCCEEEECCCC | 26.89 | 28889911 | |
| 234 | Phosphorylation | RDNLTLWTSDMSESG HCCCEEEECCCCCCC | 20.26 | 28889911 | |
| 235 | Phosphorylation | DNLTLWTSDMSESGQ CCCEEEECCCCCCCC | 21.53 | 23749301 | |
| 238 | Phosphorylation | TLWTSDMSESGQAED EEEECCCCCCCCHHH | 33.33 | 28889911 | |
| 240 | Phosphorylation | WTSDMSESGQAEDQQ EECCCCCCCCHHHHH | 28.97 | 21440633 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of BMH1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BMH1_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of BMH1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins."; Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.; Electrophoresis 18:1347-1360(1997). Cited for: ACETYLATION AT SER-2. | |
| Phosphorylation | |
| Reference | PubMed |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-66; SER-86 ANDSER-89, AND MASS SPECTROMETRY. | |
